Structure of a 6-pyruvoyltetrahydropterin synthase homolog from Streptomyces coelicolor.
The X-ray crystal structure of the 6-pyruvoyltetrahydropterin synthase (PTPS) homolog from Streptomyces coelicolor, SCO 6650, was solved at 1.5 A resolution. SCO 6650 forms a hexameric T-fold that closely resembles other PTPS proteins. The biological activity of SCO 6650 is unknown, but it lacks both a required active-site zinc metal ion and the essential catalytic triad and does not catalyze the PTPS reaction. However, SCO 6650 maintains active-site residues consistent with binding a pterin-like substrate.
Spoonamore
James E
JE
Department of Biochemistry, University of Arizona, Tucson, AZ 85721, USA.
Roberts
Sue A
SA
Heroux
Annie
A
Bandarian
Vahe
V
D001665:Binding Sites; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D019761:Phosphorus-Oxygen Lyases / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D011622:Pterins / Q000378:metabolism; D048372:Streptomyces coelicolor / Q000201:enzymology*
D011622:Pterins; D019761:Phosphorus-Oxygen Lyases; C043497:6-pyruvoyltetrahydropterin synthase